3.4.13.20: beta-Ala-His dipeptidase
This is an abbreviated version!
For detailed information about beta-Ala-His dipeptidase, go to the full flat file.
Word Map on EC 3.4.13.20
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3.4.13.20
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carnosine
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dipeptide
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nephropathy
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anserine
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homocarnosine
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beta-alanyl-l-histidine
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l-histidine
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bestatin
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n-acetylcarnosine
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histidine-containing
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carcinine
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medicine
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analysis
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synthesis
- 3.4.13.20
- carnosine
- dipeptide
- nephropathy
- anserine
- homocarnosine
- beta-alanyl-l-histidine
- l-histidine
- bestatin
-
n-acetylcarnosine
-
histidine-containing
-
carcinine
- medicine
- analysis
- synthesis
Reaction
preferential hydrolysis of the beta-Ala-/-His dipeptide (carnosine), and also anserine, Xaa-/-His dipeptides and other dipeptides including homocarnosine =
Synonyms
carnosinase, carnosinase-1, CN1, CN2, CNDP dipeptidase 2, CNDP1, CNDP2, cytosolic non-specific dipeptidase 2, DmpA, EC 3.4.13.13, EC 3.4.13.3, EC 3.4.3.3, serum carnosinase, tissue carnosinase
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General Information
General Information on EC 3.4.13.20 - beta-Ala-His dipeptidase
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malfunction
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HeLa-CN1 cells have a lower cell survival than do non-transfected cells or HeLa cells transfected with an empty or a mock vector. Viability in HeLa cells measured after H2O2 treatment is significantly higher than the viability of HeLa-CN1 cells after the same oxidant insult, indicating an increased susceptibility to oxidative stress of cells overexpressing carnosinase
metabolism
carnosine and anserine are mainly hydrolyzed by carnosinase, a low but significant amount is excreted in the urine. Carnosine reaches a steady state of very low concentration in serum, while anserine sustains higher concentrations than that of carnosine due to its greater stability vis-a-vis carnosinase after ingesting histidine-dipeptide rich diet
physiological function
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CN1 activity is lower in children and increases with age with no differences in protein concentration. CN1 activity is considerably higher in serum than in cerebrospinal fluid
physiological function
reduced glutathione, N-acetylcysteine and cysteine lower dose-dependently recombinant CN1 efficiency and normalize increased CN1 activity in renal tissue samples of diabetic mice. Inhibition is allosteric. Only cysteine-102 is influenced by cysteinylation